4PIO
Ergothioneine-biosynthetic methyltransferase EgtD in complex with N,N-dimethylhistidine and SAH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008276 | molecular_function | protein methyltransferase activity |
| A | 0032259 | biological_process | methylation |
| A | 0052699 | biological_process | ergothioneine biosynthetic process |
| A | 0052704 | biological_process | ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide |
| A | 0052706 | molecular_function | L-histidine N(alpha)-methyltransferase activity |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008276 | molecular_function | protein methyltransferase activity |
| B | 0032259 | biological_process | methylation |
| B | 0052699 | biological_process | ergothioneine biosynthetic process |
| B | 0052704 | biological_process | ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide |
| B | 0052706 | molecular_function | L-histidine N(alpha)-methyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue SAH A 401 |
| Chain | Residue |
| A | TYR39 |
| A | ASP141 |
| A | PHE142 |
| A | GLY161 |
| A | AVI402 |
| A | HOH738 |
| A | HOH740 |
| A | HOH746 |
| A | HOH753 |
| A | HOH757 |
| A | HOH759 |
| A | PHE47 |
| A | HOH783 |
| A | GLY86 |
| A | SER87 |
| A | GLY88 |
| A | LYS92 |
| A | ASP113 |
| A | VAL114 |
| A | GLY140 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue AVI A 402 |
| Chain | Residue |
| A | TYR39 |
| A | TYR56 |
| A | GLY161 |
| A | SER162 |
| A | THR163 |
| A | ASN166 |
| A | TYR206 |
| A | MET252 |
| A | GLU282 |
| A | SER284 |
| A | SAH401 |
| A | HOH772 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 403 |
| Chain | Residue |
| A | HOH851 |
| A | HOH875 |
| A | HOH885 |
| A | HOH922 |
| A | HOH973 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 404 |
| Chain | Residue |
| A | ASP233 |
| A | HOH505 |
| A | HOH556 |
| A | HOH633 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 405 |
| Chain | Residue |
| A | ASP233 |
| A | ASP235 |
| A | HOH502 |
| A | HOH625 |
| A | HOH856 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue MG A 406 |
| Chain | Residue |
| A | HOH685 |
| A | HOH689 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 407 |
| Chain | Residue |
| A | ARG218 |
| A | HIS239 |
| A | ARG257 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | binding site for residue SAH B 401 |
| Chain | Residue |
| B | LYS36 |
| B | TYR39 |
| B | PHE47 |
| B | GLY86 |
| B | SER87 |
| B | GLY88 |
| B | LYS92 |
| B | ASP113 |
| B | VAL114 |
| B | GLY140 |
| B | ASP141 |
| B | PHE142 |
| B | GLY161 |
| B | AVI402 |
| B | HOH741 |
| B | HOH742 |
| B | HOH745 |
| B | HOH746 |
| B | HOH790 |
| B | HOH791 |
| B | HOH792 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | binding site for residue AVI B 402 |
| Chain | Residue |
| B | TYR39 |
| B | TYR56 |
| B | GLY161 |
| B | SER162 |
| B | THR163 |
| B | ASN166 |
| B | TYR206 |
| B | PHE216 |
| B | MET252 |
| B | GLU282 |
| B | SER284 |
| B | SAH401 |
| B | HOH739 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue MG B 403 |
| Chain | Residue |
| B | HOH680 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 404 |
| Chain | Residue |
| B | HOH513 |
| B | HOH597 |
| B | HOH891 |
| B | HOH951 |
| site_id | AD3 |
| Number of Residues | 14 |
| Details | binding site for Ligand residues CSD A 285 through LYS A 286 bound to SER A 284 |
| Chain | Residue |
| A | PHE287 |
| A | HOH743 |
| A | HOH806 |
| A | HOH808 |
| A | HOH836 |
| A | GLY165 |
| A | LEU167 |
| A | PRO169 |
| A | ARG172 |
| A | ASP194 |
| A | TYR206 |
| A | GLU248 |
| A | ARG249 |
| A | SER284 |
| site_id | AD4 |
| Number of Residues | 14 |
| Details | binding site for Ligand residues CSD B 285 through LYS B 286 bound to SER B 284 |
| Chain | Residue |
| B | GLY165 |
| B | LEU167 |
| B | PRO169 |
| B | ARG172 |
| B | ASP194 |
| B | TYR206 |
| B | GLU248 |
| B | ARG249 |
| B | SER284 |
| B | PHE287 |
| B | HOH723 |
| B | HOH724 |
| B | HOH725 |
| B | HOH760 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25251321, ECO:0000305|PubMed:25404173, ECO:0007744|PDB:4UY6, ECO:0007744|PDB:4UY7 |
| Chain | Residue | Details |
| A | TYR56 | |
| A | ASN166 | |
| A | TYR206 | |
| A | GLU282 | |
| B | TYR56 | |
| B | ASN166 | |
| B | TYR206 | |
| B | GLU282 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:25251321, ECO:0000305|PubMed:25404173 |
| Chain | Residue | Details |
| A | GLY86 | |
| A | LYS92 | |
| A | ASP113 | |
| B | GLY86 | |
| B | LYS92 | |
| B | ASP113 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:25251321, ECO:0000305|PubMed:25404173, ECO:0007744|PDB:4PIO, ECO:0007744|PDB:4PIP, ECO:0007744|PDB:4UY6 |
| Chain | Residue | Details |
| A | ASP141 | |
| B | ASP141 |
